Aryl sulfatase of unusual specificity from the liver of marine mollusk Littorina kurila
- 1 January 2006
- journal article
- Published by Pleiades Publishing Ltd in Russian Journal of Bioorganic Chemistry
- Vol. 32 (1), 63-70
- https://doi.org/10.1134/s1068162006010067
Abstract
An aryl sulfatase of unusual specificity has been isolated from the liver of marine mollusk Littorina kurila. It hydrolyzes p-nitrophenyl sulfate, does not affect the natural fucoidan, and catalyzes splitting off the sulfate group in position C4 of xylose residues within the carbohydrate chains of holostane triterpene glycosides from sea cucumbers. The properties of the enzyme were studied at pH 5.4. The protein is homogeneous according to electrophoresis and has M 45 ± 1 kDa. The semiinactivation time of the enzyme at 60°C is 20 min, and its Km value for the hydrolysis of p-nitrophenyl sulfate is 8.7 ± 1 mM. It was shown that natural sulfated polyhydroxysteroids inhibit activity of the sulfatase; their I50 values depend on their structures and are within the range from 10−3 to 10−5 M.Keywords
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